ArticleVirology2012
Endonuclease substrate selectivity characterized with full-length PA of influenza A virus polymerase.
Article in Virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed.
- Pharmacophores of Influenza Virus PA Endonuclease Inhibitors.Advances in experimental medicine and biology · 2026Review
- The search for an antiviral lead molecule to combat the neglected emerging Oropouche virus.Current research in microbial sciences · 2024Article
- Acridones as promising drug candidates against Oropouche virus.Current research in microbial sciences · 2024Article
- Article
- Enzymatic Assays to Explore Viral mRNA Capping Machinery.Chembiochem : a European journal of chemical biology · 2021Review
- Molecular Docking and Virtual Screening of an Influenza Virus Inhibitor That Disrupts Protein-Protein Interactions.Viruses · 2021Article
- The Cap-Snatching SFTSV Endonuclease Domain Is an Antiviral Target.Cell reports · 2020Article
- Flupyranochromene, a novel inhibitor of influenza virus cap-dependent endonuclease, from Penicillium sp. f28743.The Journal of antibiotics · 2019Article
- Focusing on the Influenza Virus Polymerase Complex: Recent Progress in Drug Discovery and Assay Development.Current medicinal chemistry · 2019Review
- Crystal structures ofIUCrJ · 2018Article
- Article
- Amino acid substitutions V63I or A37S/I61T/V63I/V100A in the PA N-terminal domain increase the virulence of H7N7 influenza A virus.Scientific reports · 2016Article
- The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug Design.Medicinal research reviews · 2016Review
- Identification and characterization of influenza variants resistant to a viral endonuclease inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A novel small-molecule inhibitor of influenza A virus acts by suppressing PA endonuclease activity of the viral polymerase.Scientific reports · 2016Article
- Article
- The novel influenza A virus protein PA-X and its naturally deleted variant show different enzymatic properties in comparison to the viral endonuclease PA.Nucleic acids research · 2015Article
- Cross-protection of influenza A virus infection by a DNA aptamer targeting the PA endonuclease domain.Antimicrobial agents and chemotherapy · 2015Article
- An integrated biological approach to guide the development of metal-chelating inhibitors of influenza virus PA endonuclease.Molecular pharmacology · 2015Article
- Bat-derived influenza-like viruses H17N10 and H18N11.Trends in microbiology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The influenza A polymerase is a heterotrimer which transcribes viral mRNAs and replicates the viral genome. To initiate synthesis of mRNA, the polymerase binds a host pre-mRNA and cleaves a short primer downstream of the 5' end cap structure. The N-terminal domain of PA has been demonstrated to have endonuclease activity in vitro. Here we sought to better understand the biochemical nature of the PA endonuclease by developing an improved assay using full-length PA protein. This full-length protein is active against both RNA and DNA in a cap-independent manner and can use several different divalent cations as cofactors, which affects the secondary structure of the full-length PA. Our in vitro assay was also able to demonstrate the minimal substrate size and sequence selectivity of the PA protein, which is crucial information for inhibitor design. Finally, we confirmed the observed endonuclease activity of the full-length PA with a FRET-based assay.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.